Nitrilases are a class of enzymes capable of converting nitriles to it corresponding carboxylic acids with the release of ammonia. In some instances, the enzymes release an amide product (Fernandes et al., 2006, Adv Synth Catal 348, 2597-2603). Their high chemical specificity and frequent enantioselectivity makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates, such as -amino-, -hydroxy- or -methylcarboxylic acids. A nitrile group offers advantages in devising synthetic routes in that it is often easily introduced into a molecular structure and can be carried through many processes as a masked acid or amide group. However, their conversion to corresponding amides and carboxylic acids requires harsh conditions and generates significant chemical waste. Enzymatic hydrolysis of nitriles can be performed under mild conditions and can also take advantage of stereospecific enzymatic hydrolysis and nitrile reracemization to provide highly enantioselective conversions. Nitrilases that act on aromatic or aliphatic nitriles have been described. Given the utility of these enzymes, it is desirable to identify nitrilases with performance characteristics that make them applicable to a variety of reaction conditions and substrates.